人类红细胞中的吡咯啉-5-羧酸还原酶。
Pyrroline-5-carboxylate reductase in human erythrocytes.
作者信息
Yeh G C, Harris S C, Phang J M
出版信息
J Clin Invest. 1981 Apr;67(4):1042-6. doi: 10.1172/jci110115.
Abstract
Pyrroline-5-carboxylate reductase, which converts pyrroline-5-carboxylate to proline, has been identified in human erythrocytes. The level of pyrroline-5-carboxylate reductase activity in these cells is comparable to the activity levels of major erythrocyte enzymes. The physiologic function of the enzyme in erythrocytes cannot be related to its function in other tissues, i.e., producing proline for protein synthesis. We examined the kinetic properties of erythrocyte pyrroline-5-carboxylate reductase and compared them to the properties of the enzyme from proliferating cultured human fibroblasts. We found that the kinetic properties and regulation of the erythrocyte enzyme are distinctly different from those for human fibroblast pyrroline-5-carboxylate reductase. These characteristics are consistent with the interpretation that the function of the enzyme in human erythrocytes may be to generate oxidizing potential in the form of NADP+.
摘要
在人红细胞中已鉴定出将吡咯啉 - 5 - 羧酸转化为脯氨酸的吡咯啉 - 5 - 羧酸还原酶。这些细胞中吡咯啉 - 5 - 羧酸还原酶的活性水平与主要红细胞酶的活性水平相当。该酶在红细胞中的生理功能与其在其他组织中的功能无关，即在其他组织中该酶为蛋白质合成产生脯氨酸。我们研究了红细胞吡咯啉 - 5 - 羧酸还原酶的动力学特性，并将其与来自增殖培养的人成纤维细胞的该酶特性进行比较。我们发现红细胞酶的动力学特性和调节与人类成纤维细胞吡咯啉 - 5 - 羧酸还原酶明显不同。这些特征与以下解释一致，即该酶在人红细胞中的功能可能是以NADP⁺的形式产生氧化电位。
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